Two β-glucosidases from Candida wickerhamii were studied. One is parietal and exocellular, the other is endocellular. Both enzymes were purified by ion-exchange chromatography and gel filtration. They could hydrolyze glucosides with β(1-3), β(1-4) and β(1-6) configurations. The exocellular enzyme is active against soluble cellodextrins (D.P 3 to 6). This is responsible for the ability of the Candida wickerhamii strain to ferment soluble cellodextrins. Both enzymes were constitutive, but their biosynthesis was repressed by glucose.
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Leclerc et al. (1984) studied this question.